Magnesium in PDB 5wmt: Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim.

The structure of Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim., PDB code: 5wmt was solved by N.S.Que, D.T.Gewirth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.54 / 2.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	94.412, 94.730, 179.250, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 23.7

The structure of Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim. also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Magnesium atom in the Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim. (pdb code 5wmt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim., PDB code: 5wmt:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg404 b:82.0 occ:1.00 NE1 B:TRP282 3.2 75.9 1.0 CD2 B:TRP331 3.5 87.2 1.0 CG B:TRP331 3.6 86.7 1.0 CE2 B:TRP331 3.6 85.3 1.0 CD1 B:TRP331 3.7 86.0 1.0 NE1 B:TRP331 3.8 84.4 1.0 CD1 B:TRP282 3.8 77.4 1.0 CE3 B:TRP331 4.0 79.2 1.0 CB B:TRP331 4.2 80.3 1.0 CZ2 B:TRP331 4.2 87.6 1.0 CE2 B:TRP282 4.5 76.2 1.0 CZ3 B:TRP331 4.5 82.9 1.0 CH2 B:TRP331 4.6 88.6 1.0

Magnesium binding site 2 out of 2 in the Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of GRP94 N-Terminal Domain Bound to Resorcinylic Inhibitor Bnim. within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg405 b:85.3 occ:1.00 NE1 C:TRP282 3.3 80.2 1.0 CD2 C:TRP331 3.6 87.8 1.0 CG C:TRP331 3.7 86.5 1.0 CE2 C:TRP331 3.8 82.1 1.0 CD1 C:TRP282 3.9 77.5 1.0 CD1 C:TRP331 4.0 87.9 1.0 CE3 C:TRP331 4.0 81.9 1.0 NE1 C:TRP331 4.0 84.1 1.0 CB C:TRP331 4.4 83.9 1.0 CZ2 C:TRP331 4.4 81.2 1.0 CE2 C:TRP282 4.5 80.0 1.0 CZ3 C:TRP331 4.5 82.2 1.0 CH2 C:TRP331 4.7 89.4 1.0 CE C:LYS137 4.8 84.5 1.0

N.L.S.Que, V.M.Crowley, A.S.Duerfeldt, J.Zhao, C.N.Kent, B.S.J.Blagg, D.T.Gewirth. Structure Based Design of A GRP94-Selective Inhibitor: Exploiting A Key Residue in GRP94 to Optimize Paralog-Selective Binding. J. Med. Chem. V. 61 2793 2018.
ISSN: ISSN 1520-4804
PubMed: 29528635
DOI: 10.1021/ACS.JMEDCHEM.7B01608